Also known as DPCK, NBIA6, NBP, PPAT, UKR1, pOV-2, Coenzyme A synthase, PCH12
Bifunctional coenzyme A synthase is an enzyme that in mammals is encoded by the COASY gene that catalyses the synthesis of coenzyme A from 4'-phosphopantetheine.
Coenzyme A (CoA) functions as a carrier of acetyl and acyl groups in cells and thus plays an important role in numerous synthetic and degradative metabolic pathways in all organisms. In eukaryotes, CoA and its derivatives are also involved in membrane trafficking and signal transduction. This gene encodes the bifunctional protein coenzyme A synthase (CoAsy) which carries out the last two steps in the biosynthesis of CoA from pantothenic acid (vitamin B5). The phosphopantetheine adenylyltransferase domain of this bifunctional protein catalyzes the conversion of 4'-phosphopantetheine into dephospho-coenzyme A (dpCoA) while its dephospho-CoA kinase domain completes the final step by phosphorylating dpCoA to form CoA. Mutations in this gene are associated with neurodegeneration with brain iron accumulation (NBIA). Alternative splicing results in multiple isoforms. [provided by RefSeq, Apr 2014].
via MyGene.info
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Bifunctional coenzyme A synthase is an enzyme that in mammals is encoded by the COASY gene that catalyses the synthesis of coenzyme A from 4'-phosphopantetheine.
== Function == COASY is an enzyme that catalyzes the last two steps in the synthesis of coenzyme A from vitamin B5 (pantothenic acid). The primary substrate is 4'-phosphopantetheine and COASY is a bifunctional enzyme in this pathway: 4′-Phosphopantetheine is adenylated to form dephospho-CoA by the enzyme phosphopantetheine adenylyl-transferase (PPAT; CoaD) Next, dephospho-CoA is phosphorylated to coenzyme A by the enzyme dephospho-CoA kinase (DPCK; CoaE) In mammals this is a single enzyme, but in organisms including yeast and bacteria these enzymes are encoded by separate genes. == Interactions == COASY has been shown to interact with P70-S6 Kinase 1. In 2009, COASY has also been implicated in PI3K signaling, as it was shown to interact with a regulatory subunit of PI3K.
Discovered by embedding cosine similarity (sentence-transformers MiniLM, 384-dim).